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J Biol Chem, Vol. 273, Issue 10, 5443-5446, March 6, 1998
From the Departments of Pediatrics, Physiology, Nuclear Medicine,
and Molecular Genetics-Microbiology and the Cancer Center, University
of Medical Center, Worcester, Massachusetts 01605
Prokaryotic and eukaryotic cells incorporate the
unusual amino acid selenocysteine at a UGA codon, which conventionally
serves as a termination signal. Translation of eukaryotic selenoprotein mRNA requires a nucleotide selenocysteine insertion sequence in the
3'-untranslated region. We report the molecular cloning of the binding
protein that recognizes the selenocysteine insertion sequence element
in human cellular glutathione peroxidase gene (GPX1)
transcripts and its identification as DNA-binding protein B, a member
of the EFIA/dbpB/YB-1 family. The predicted amino acid
sequence contains four arginine-rich RNA-binding motifs, and one
segment shows strong homology to the human immunodeficiency virus Tat
domain. Recombinant DNA-binding protein B binds the selenocysteine
insertion sequence elements from the GPX1 and type I
iodothyronine 5'-deiodinase genes in RNA electrophoretic mobility shift
assays and competes with endogenous GPX1 selenocysteine insertion sequence binding activity in COS-1 cytosol extracts. Addition
of antibody to DNA-binding protein B to COS-1 electromobility shift
assays produces a slowly migrating "supershift" band. The molecular
cloning and identification of DNA-binding protein B as the first
eukaryotic selenocysteine insertion sequence-binding protein opens the
way to the elucidation of the entire complex necessary for the
alternative reading of the genetic code that permits translation of
selenoproteins.
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